Two sorts of oxygenases prosthetic groups have been shown to incorporate one, or two, atoms of oxygen from the molecular state into organic substrates. The best understood today employ flavoprotein or b- type cytochromes, protein 450 (P450). The effector or reductive transport chains may also differ - flavine, iron sulfur and pteridine proteins. A number of other systems are known in biology that incorporate molecular oxygen into organic molecules, e.g., the ketolactonases I and II of the bicyclic monoterpene camphor, the analogous oxygenative cleavage of the D-ring of the steroid nucleus, etc. Some evidence points to ferrous iron requirements for other oxygenases of both the monoxygenase and dioxygenase class. Several biological reactions that oxygenate chemicals potentially toxic to plant or animal life have been explored in a perfunctory way. We should like to explore in more depth the oxygenation by apparent monoxygenases of the substituted secondary and tertiary amines, e.g., nitrilotriacetate (NTA). Preliminary experiments and cultures are at hand. The stereochemistry of the 1,3 diketone pathway of bicyclic monoterpene oxygenation is subject to attack by the methods previously applied with initial data indicative of a 6-endo hydroxylation with one enzyme selective for both the D and L enantiomors. The question of oxygenases at later stage of these metabolic processes is open and subject to exploration. The management of biological systems for isotope substitution is actively underway for selenium, cobalt and iron. Preparation of these systems for analysis of the structure and interaction of components and the reaction mechanisms will be the primary focus of our experiments for the coming year.